Association of the parainfluenza virus fusion and hemagglutinin-neuraminidase glycoproteins on cell surfaces.
about
Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion.Efficacy of novel hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 against human parainfluenza viruses in vitro and in vivoBimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggeringParainfluenza virusesMembrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins.Structure and Mutagenesis of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Stalk Domain Reveals a Four-Helix Bundle and the Role of the Stalk in Fusion PromotionChimeric bovine respiratory syncytial virus with attachment and fusion glycoproteins replaced by bovine parainfluenza virus type 3 hemagglutinin-neuraminidase and fusion proteinsActivation of paramyxovirus membrane fusion and virus entryN-linked glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site.A recombinant measles vaccine virus expressing wild-type glycoproteins: consequences for viral spread and cell tropism.Hemagglutinin-neuraminidase-independent fusion activity of simian virus 5 fusion (F) protein: difference in conformation between fusogenic and nonfusogenic F proteins on the cell surface.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Mutations in the stalk region of the measles virus hemagglutinin inhibit syncytium formation but not virus entry.Probing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies.Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion.The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (HN) protein: an HN mutation diminishes the rate of F activation and fusionRoles of the fusion and hemagglutinin-neuraminidase proteins in replication, tropism, and pathogenicity of avian paramyxoviruses.Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Quantitative analysis of Nipah virus proteins released as virus-like particles reveals central role for the matrix protein.Detection of an interaction between the HN and F proteins in Newcastle disease virus-infected cells.Paramyxovirus fusion and entry: multiple paths to a common endMutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein.Type II integral membrane protein, TM of J paramyxovirus promotes cell-to-cell fusion.Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.Interacting domains of the HN and F proteins of newcastle disease virus.Effect of hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 on growth and pathogenicity of Sendai/human parainfluenza type 3 chimera virus in mice.Mutations in the parainfluenza virus 5 fusion protein reveal domains important for fusion triggering and metastability.Efficacy of the novel parainfluenza virus haemagglutinin-neuraminidase inhibitor BCX 2798 in mice - further evaluation.Amino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein.Viral entry mechanisms: the increasing diversity of paramyxovirus entry.Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state.Fusion activation through attachment protein stalk domains indicates a conserved core mechanism of paramyxovirus entry into cellsDecreased dependence on receptor recognition for the fusion promotion activity of L289A-mutated newcastle disease virus fusion protein correlates with a monoclonal antibody-detected conformational changeInfection of ciliated cells by human parainfluenza virus type 3 in an in vitro model of human airway epithelium.Identification of Interferon-Stimulated Gene Proteins That Inhibit Human Parainfluenza Virus Type 3Functional interaction between paramyxovirus fusion and attachment proteins.Importance of the cytoplasmic tails of the measles virus glycoproteins for fusogenic activity and the generation of recombinant measles viruses.Glycoprotein interactions in paramyxovirus fusion.Identification of Hendra virus G glycoprotein residues that are critical for receptor binding.
P2860
Q24538786-E50CB5AE-8645-4AE1-8909-C35C3421290FQ24567591-3A63FDF9-50D4-4103-95A3-9E13EBDA8535Q24645164-78533E0E-266B-4F91-8749-9B46BE42F2B9Q24682952-F5ECAFCA-E7C4-4156-8749-F7A262C6006EQ27472931-38E30EEC-C472-47A0-80F5-E60007DB3C8BQ27674994-6C6FB573-4E86-41C7-B937-2FB9864466C3Q30708312-3D0E4684-754F-4A9A-A9C7-2D5BB87DAA9BQ33638769-BF97F137-0270-48B5-A0ED-5F04B158B6C3Q33676467-1C81B78A-2BCB-4B41-ADA5-CD85497F8489Q33817891-C7853709-F4A8-496F-B9F9-A4CD7F66882DQ33845134-B6773F55-9204-4C63-848E-C1AC726E3AB6Q34102261-8F3E1299-2FE0-424E-BFAF-172AA91E7C18Q34178182-BB7DA306-6A89-4A84-B0B2-B843106BB3BDQ34261586-F88EC332-BADB-4B49-9B46-D2F2435A493EQ34301817-A0DAF2BD-078E-4690-BF2A-62E26B158566Q34742453-E43B3B44-4972-4298-8C17-FB7194CF168BQ34745220-0B009AF3-6CBA-4878-A4E4-E9EDD49F26A5Q35192881-E4397507-2552-4021-BC14-51E8788E8DAFQ35582400-CD959F74-3129-4EAE-9279-BF9E545B76FDQ35608833-B792A5EB-D07E-4317-B27A-E05DF20DD5DCQ35890850-E4F8B54D-0D08-4764-B875-ABA9039AAF3DQ35943669-A1681598-ED4F-4405-A0C0-245FFD0824D4Q36098830-47B98580-52CA-45C3-AC08-A115CF200DF8Q36155057-8AAD6C9A-002E-4FD1-A80C-07704C7AB9C8Q36300779-614737B1-9120-4E80-B347-CE9E9150FFBBQ36474158-6227BFF6-0B1E-4B99-B902-3C7CDCA7AD4FQ37333181-C462D185-6F66-47B1-A27F-015D6278511CQ37336715-1AD87C17-3F1D-4958-83BE-D413FA07311DQ37436674-A683484C-C04C-4F4B-AFAB-FA6088B3731DQ37596488-00687D1A-F5B6-45CC-BE90-845ACA999835Q37624858-8DFDA888-4E14-4AA2-A134-5E8594482818Q37683548-14EEA4C2-F8C0-48B6-9C8A-BCF4CE106EF9Q37713834-DB3FB73E-0B53-4CB3-A376-6DE0A47359A4Q37743253-31E67CB1-B7BE-4F96-A910-2859615481C2Q37743793-3B465CC8-D43C-4A2C-8521-F3D17AF0B100Q38735173-DFAFDB52-8118-46FD-96DC-65C583927168Q39026212-B1EB812F-039B-4D57-9632-7E88B2C5F451Q39684160-87A94F41-0B03-4418-A0CB-E379E62AAB4AQ39900113-159CD414-D65E-4C1F-BA6F-5B4370D69527Q40155851-B198CAC3-0902-416F-B21F-9CD581EB5B02
P2860
Association of the parainfluenza virus fusion and hemagglutinin-neuraminidase glycoproteins on cell surfaces.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Association of the parainfluen ...... lycoproteins on cell surfaces.
@ast
Association of the parainfluen ...... lycoproteins on cell surfaces.
@en
type
label
Association of the parainfluen ...... lycoproteins on cell surfaces.
@ast
Association of the parainfluen ...... lycoproteins on cell surfaces.
@en
prefLabel
Association of the parainfluen ...... lycoproteins on cell surfaces.
@ast
Association of the parainfluen ...... lycoproteins on cell surfaces.
@en
P2093
P2860
P1433
P1476
Association of the parainfluen ...... lycoproteins on cell surfaces.
@en
P2093
P2860
P304
P407
P577
1997-01-01T00:00:00Z